Team:Hong Kong CUHK/abstract

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  <p>  <strong>  Polycyclic  aromatic hydrocarbons (PAHs) are harmful to both environment and human health.  We proposed the PAHs degradation system, which contains codon-optimized laccase  from Bacillus sp. HR03 and catechol 1,2-dioxygenase from Pseudomonas putida  KT2440 for Escherichia coli. The system was capable of degrading PAHs into less  toxic simple carboxylic acid. Also, since quinones are intermediates in the  pathway, we added quinone sensing and response repressor (QsrR) to regulate the  degradation process. To accelerate the degradation, we used Voltage Switch  (VS), the other great highlight of our project. We designed a novel  transmembrane protein called Voltage Switch (VS), which is a fusion protein utilizing the voltage sensing domain from potassium ion channels. Triggered by change in potential across the cell membrane, VS can separate or bring  targeting enzymes into proximity; thus allowing an instant control of enzymatic reaction.</strong></p>
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   To rapidly regulate biological process, we designed a novel  transmembrane protein called Voltage Switch (VS),&nbsp;which is a&nbsp;fusion  protein utilizing the voltage sensing domain from potassium ion channels. Triggered by a change of potential across the&nbsp;inner membrane, VS can bring  targeting enzymes into proximity, thus allowing an instant control of  enzymatic&nbsp;reaction. We also utilized VS to accelerate the polycyclic  aromatic hydrocarbons (PAHs) degradation system — another&nbsp;highlight of our  project. The metabolites of certain PAHs are mutagenic and carcinogenic. We  codon-optimized laccase from&nbsp;<em>Bacillus  sp</em>. HR03 and catechol 1,2-dioxygenase from <em>Pseudomonas putida</em> KT2440 for <em>Escherichia  coli</em>, which when forming&nbsp;a cascade, can degrade PAHs into less toxic  simple carboxylic acid. For regulation, we added quinone sensing and response  repressor (QsrR) to control the degradation, as quinones are intermediates in  the pathway. </p>
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Latest revision as of 15:24, 28 October 2013

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